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Ca9Y(VO4)7 phosphor activated with Er3+ ions have been developed by the urea-aided solution combustion technique. XRD profiles assisted with Rietveld refinement executed over-developed Er3+-activated Ca9Y(VO4)7 powder, revealed a trigonal phase with the R3c space group. The electron microscope techniques namely TEM and SEM characterize the size and surface-linked qualities of the developed nanopowder, respectively. The uniform distribution of various elements in the nanocrystalline sample is authenticated by an energy-dispersive spectroscopy (EDS) system. The Eg (band gap) value of 3.64 eV for Ca9Y0.9Er0.1(VO4)7 and 3.74 eV for Ca9Y(VO4)7 has been estimated. Upon 382 nm excitation, Er3+: Ca9Y(VO4)7 phosphor gives rise to the bright green emission owing to the 4S3/2 → 4I15/2 transition. The concentration quenching after 10 mol% composition of trivalent erbium ions is attributed to dipole-dipole interlinkages in accordance with Dexter's theory. The radiative lifetime (1.1083 ms), non-radiative rates (0.2079 ms− 1), quantum efficiency (79%), along with colorimetric parameters i.e. CIE x (= 0.2577), y (= 0.4566), and CCT quantities offer Ca9Y0.9Er0.1(VO4)7 as a proficient green radiating nanomaterial for RGB phosphors in solid-state applications. [ABSTRACT FROM AUTHOR]

Diversely substituted methoxy derivatives of arylpiperazinyl–alkyl benzothiazolone has been evaluated as specific probe for 5HT7. To determine the best methoxy derivative for 5HT7 receptor affinity, we synthesised a number of 2-benzothiazolone arylalkyl piperazine derivatives. In-vitro/vivo studies with C-2 substituted [11C]ABT showed 5HT7 specific binding. The radiochemical purity of [11C]ABT was found to be more than 99% with radiochemical stability persistence for more than 1.5 hr at 25 °C. The interaction of BSA and ABT has been analysed by photophysical studies for better understanding of properties such as adsortion, distribution, metabolism and elemination (ADME). The interaction between ABT and BSA was analyzed by using the UV-vis and fluorescence spectra. UV-vis spectra analyzed the changes in primary structure of BSA on its interaction with ABT. ABT showed quenched fluorescence emission intensity of tryptophan residues in BSA via static quenching mechanism. This study might help to understand how ABT binds to serum protein or subsequently to know the ADME of this drug candidate. [ABSTRACT FROM AUTHOR]